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PMID: 9087509 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases.

Antimicrobial agents and chemotherapy ·Vol. 41 ·No. 4 ·1997-04-00 ·Pages 866-8

Felici A, Perilli M, Franceschini N, Rossolini GM, Galleni M, Frere JM, Oratore A, Amicosante G

Abstract

Ceftriaxone and ceftriaxone S-oxide behaved as inactivators against the metallo-beta-lactamase of Aeromonas hydrophila AE036 and as substrates for the zinc beta-lactamase produced by Bacillus cereus (569/H/9) and Stenotrophomonas maltophilia ULA 511. Moreover, RO 09-1428, a catechol-cephalosporin, was not recognized by the A. hydrophila enzyme. Panipenem, cephalosporin C, cephalosporin C-gamma-lactone, and loracarbef were substrates for the three studied beta-lactamases.

MeSH Terms

Aeromonas hydrophila/drug effects,enzymology Bacterial Proteins Cyclosporins/pharmacology Enzyme Inhibitors/pharmacology Hydrolysis Kinetics beta-Lactamase Inhibitors beta-Lactamases

Chemicals

Bacterial Proteins Cyclosporins Enzyme Inhibitors beta-Lactamase Inhibitors beta-Lactamases carbapenemase

Authors & Affiliations

8 authors, click to expand affiliations / ORCID

Felici A

Dipartimento di Scienze e Tecnologie Biomediche Cattedra di Chimica Biologica e di Enzimologia, Università degli Studi dell'Aquila, Coppito (L'Aquila), Italy.

Perilli M

Franceschini N

Rossolini G M

Galleni M

Frere J M

Oratore A

Amicosante G

References (10)

10 references, click to expand

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Article Info

Journal

Antimicrobial agents and chemotherapy

Abbr.

Antimicrob Agents Chemother

ISSN

0066-4804

DOI

10.1128/AAC.41.4.866

Published

1997-04-00

Pages

866-8

Language

English

Region

United States

NLM ID

0315061

PMCID

PMC163814

Subset

External Links

PubMed source DOI: 10.1128/AAC.41.4.866 PMC Full Text View journal details

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Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases.

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